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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
3
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pubmed:dateCreated |
2007-8-24
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pubmed:abstractText |
The Arabidopsis acn (acetate non-utilizing) mutants were isolated by fluoroacetate-resistant germination and seedling establishment. We report the characterization of the acn2 mutant. Physiological analyses of acn2 showed that it possessed characteristics similar to those of the mutants cts (COMATOSE)-1 and pxa [peroxisomal ABC (ATP-binding-cassette) transporter]1. The acn2 locus was mapped to within 3 cM of the CTS gene on the bottom arm of chromosome IV using CAPS (cleavage amplification polymorphism) and SSLP (simple sequence-length polymorphism) markers. Crossing acn2 and cts-1 failed to restore the fluoroacetate-sensitive phenotype, suggesting that these mutations were allelic. Sequencing of the ACN2 locus revealed a C-->T nonsense mutation in exon 13, which would have resulted in the elimination of the C-terminal hemitransporter domain of the encoded protein. Neither the full-length CTS protein nor the truncated protein was detected on immunoblots using either C-terminal- or N-terminal-specific anti-CTS antibodies respectively, demonstrating the absence of the entire CTS protein in acn2 mutants. Emerged seedlings of both cts-1 and pxa1 alleles displayed increased resistance to FAc (monofluoroacetic acid) compared with the corresponding wild-type seedlings. Complementation studies showed that mutation of the CTS gene was responsible for the FAc-resistant phenotype, as when the wild-type protein was expressed in both the cts-1 and pxa1 mutant lines, the strains became FAc-sensitive. Feeding studies confirmed that both acn2 and cts-1 mutants were compromised in their ability to convert radiolabelled acetate into soluble carbohydrate. These results demonstrate a role for the ABC protein CTS in providing acetate to the glyoxylate cycle in developing seedlings.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-10207018,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-10227685,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-10805817,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-10934020,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-11063705,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-11449047,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-11696182,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-11706205,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-11828016,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-12029478,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-12805634,
http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-13159282,
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http://linkedlifedata.com/resource/pubmed/commentcorrection/17581114-9490742
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Sep
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pubmed:issn |
1470-8728
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:day |
15
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pubmed:volume |
406
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
399-406
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pubmed:dateRevised |
2009-11-18
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pubmed:meshHeading |
pubmed-meshheading:17581114-ATP-Binding Cassette Transporters,
pubmed-meshheading:17581114-Acetates,
pubmed-meshheading:17581114-Arabidopsis,
pubmed-meshheading:17581114-Arabidopsis Proteins,
pubmed-meshheading:17581114-Cell Line,
pubmed-meshheading:17581114-Codon, Nonsense,
pubmed-meshheading:17581114-Fatty Acid Transport Proteins,
pubmed-meshheading:17581114-Gene Expression Regulation, Plant,
pubmed-meshheading:17581114-Germination,
pubmed-meshheading:17581114-Peroxisomes,
pubmed-meshheading:17581114-Phenotype,
pubmed-meshheading:17581114-Plants, Genetically Modified,
pubmed-meshheading:17581114-Seedling
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pubmed:year |
2007
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pubmed:articleTitle |
The Arabidopsis ALDP protein homologue COMATOSE is instrumental in peroxisomal acetate metabolism.
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pubmed:affiliation |
School of Biological Sciences, University of Wales Bangor, Bangor, Gwynedd LL57 2UW, Wales, UK. m.a.hooks@bangor.ac.uk
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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